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000094235 1001_ $$aCao, X.
000094235 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000094235 245__ $$aGolgi protein FAPP2 tubulates membranes
000094235 260__ $$aWashington, DC$$bAcademy$$c2009
000094235 300__ $$a21121-21125
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000094235 440_0 $$0PERI:(DE-600)1461794-8$$aProc. Nat. Acad. Sci. USA$$v106$$x1091-6490
000094235 500__ $$3Converted on 2013-05-30 14:57
000094235 500__ $$3Converted on 2013-06-21 19:21
000094235 520__ $$aThe Golgi-associated four-phosphate adaptor protein 2 (FAPP2) has been shown to possess transfer activity for glucosylceramide both in vitro and in cells. We have previously shown that FAPP2 is involved in apical transport from the Golgi complex in epithelial MDCK cells. In this paper we assign an unknown activity for the protein as well as providing structural insight into protein assembly and a low-resolution envelope structure. By applying analytical ultracentrifugation and small-angle x-ray scattering, we show that FAPP2 is a dimeric protein in solution, having a curved shape 30 nm in length. The purified FAPP2 protein has the capability to form tubules from membrane sheets in vitro. This activity is dependent on the phosphoinositide-binding activity of the PH domain of FAPP2. These data suggest that FAPP2 functions directly in the formation of apical carriers in the trans-Golgi network.
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000094235 650_7 $$00$$2NLM Chemicals$$aAdaptor Proteins, Signal Transducing
000094235 650_7 $$00$$2NLM Chemicals$$aLipid Bilayers
000094235 650_7 $$00$$2NLM Chemicals$$aPLEKHA8 protein, human
000094235 650_7 $$00$$2NLM Chemicals$$aPhosphatidylinositols
000094235 650_7 $$00$$2NLM Chemicals$$aSolutions
000094235 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: chemistry
000094235 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: metabolism
000094235 650_2 $$2MeSH$$aAdaptor Proteins, Signal Transducing: physiology
000094235 650_2 $$2MeSH$$aAnimals
000094235 650_2 $$2MeSH$$aCell Line
000094235 650_2 $$2MeSH$$aDogs
000094235 650_2 $$2MeSH$$aLipid Bilayers: metabolism
000094235 650_2 $$2MeSH$$aPhosphatidylinositols: metabolism
000094235 650_2 $$2MeSH$$aProtein Binding
000094235 650_2 $$2MeSH$$aProtein Conformation
000094235 650_2 $$2MeSH$$aProtein Multimerization
000094235 650_2 $$2MeSH$$aSolutions
000094235 650_2 $$2MeSH$$atrans-Golgi Network
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000094235 7001_ $$aCoskun, Ü.
000094235 7001_ $$aRössle, M.
000094235 7001_ $$aBuschhorn, S. B.
000094235 7001_ $$aGrzybek, M.
000094235 7001_ $$aDafforn, T. R.
000094235 7001_ $$aLenoir, M.
000094235 7001_ $$aOverduin, M.
000094235 7001_ $$aSimons, K.
000094235 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.0911789106$$gVol. 106, p. 21121-21125$$p21121-21125$$q106<21121-21125$$tProceedings of the National Academy of Sciences of the United States of America$$v106$$x1091-6490$$y2009
000094235 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2795549
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000094235 9141_ $$a(c) National Academy of Sciences.$$y2009
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